Glycosylation of the West Nile Virus Envelope Protein Increases In Vivo and In Vitro Viral Multiplication in Birds

Many West Nile (WN) virus isolates associated with significant outbreaks possess a glycosylation site on the envelope (E) protein. E-protein glycosylated variants of New York (NY) strains of WN virus are more neuroinvasive in mice than the non-glycosylated variants. To determine how E protein glycos...

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Bibliographic Details
Published in:The American journal of tropical medicine and hygiene 2010-04, Vol.82 (4), p.696-704
Main Authors: Murata, Ryo, Eshita, Yuki, Maeda, Akihiko, Maeda, Junko, Akita, Saki, Tanaka, Tomohisa, Yoshii, Kentaro, Kariwa, Hiroaki, Umemura, Takashi, Takashima, Ikuo
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Cell Line
Chickens
Cricetinae
Culex
Female
Genes, Viral
Glycosylation
Infectious diseases
Male
Medical sciences
Muscle Cells - pathology
Muscle Cells - virology
Mutation
Poultry Diseases - virology
Viral Envelope Proteins - genetics
Viral Envelope Proteins - metabolism
Viremia
Virus Replication - physiology
West Nile Fever - pathology
West Nile Fever - veterinary
West Nile Fever - virology
West Nile virus - pathogenicity
West Nile virus - physiology
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Summary:Many West Nile (WN) virus isolates associated with significant outbreaks possess a glycosylation site on the envelope (E) protein. E-protein glycosylated variants of New York (NY) strains of WN virus are more neuroinvasive in mice than the non-glycosylated variants. To determine how E protein glycosylation affects the interactions between WN virus and avian hosts, we inoculated young chicks with NY strains of WN virus containing either glycosylated or non-glycosylated variants of the E protein. The glycosylated variants were more virulent and had higher viremic levels than the non-glycosylated variants. The glycosylation status of the variant did not affect viral multiplication and dissemination in mosquitoes in vivo. Glycosylated variants showed more heat-stable propagation than non-glycosylated variants in mammalian (BHK) and avian (QT6) cells but not in mosquito (C6/36) cells. Thus, E-protein glycosylation may be a requirement for efficient transmission of WN virus from avian hosts to mosquito vectors.
ISSN:0002-9637
1476-1645
DOI:10.4269/ajtmh.2010.09-0262